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The C-terminal 19-kDa domain of merozoite surface protein 1 (MSP119 ) is the target of protective antibodies but alone is poorly immunogenic. Previously, using thePlasmodium yoelii murine model, we fusedP. yoelii MSP119 (Py MSP119 ) with full-lengthP. yoelii merozoite surface protein 8 (MSP8). Upon immunization, the MSP8-restricted T cell response provided help for the production of high and sustained levels of protectivePy MSP119 - andPy MSP8-specific antibodies. Here, we assessed the vaccine potential of MSP8 of the human malaria parasite,Plasmodium falciparum . Distinct fromPy MSP8,P. falciparum MSP8 (Pf MSP8) contains an N-terminal asparagine and aspartic acid (Asn/Asp)-rich domain whose function is unknown. Comparative analysis of recombinant full-lengthPf MSP8 and a truncated version devoid of the Asn/Asp-rich domain,Pf MSP8(ΔAsn/Asp), showed that both proteins were immunogenic for T cells and B cells. All T cell epitopes utilized mapped within rPf MSP8(ΔAsn/Asp). The dominant B cell epitopes were conformational and common to both rPf MSP8 and rPf MSP8(ΔAsn/Asp). Analysis of nativePf MSP8 expression revealed thatPf MSP8 is present intracellularly in late schizonts and merozoites. Following invasion,Pf MSP8 is found distributed on the surface of ring- and trophozoite-stage parasites. Consistent with a low and/or transient expression ofPf MSP8 on the surface of merozoites,Pf MSP8-specific rabbit IgG did not inhibit thein vitro growth ofP. falciparum blood-stage parasites. These studies suggest that the further development ofPf MSP8 as a malaria vaccine component should focus on the use ofPf MSP8(ΔAsn/Asp) and its conserved, immunogenic T cell epitopes as a fusion partner for protective domains of poor immunogens, includingPf MSP119 .

Evaluation of the Immunogenicity and Vaccine Potential of Recombinant Plasmodium falciparum Merozoite Surface Protein 8